ID   SLA_ECHCA               Reviewed;         135 AA.
AC   Q7T248;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Snaclec echicetin subunit alpha;
DE   Flags: Precursor; Fragment;
OS   Echis carinatus (Saw-scaled viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=40353;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 5-135,
RP   AND DISULFIDE BONDS.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=14659748; DOI=10.1016/j.jmb.2003.10.048;
RA   Jasti J., Paramasivam M., Srinivasan A., Singh T.P.;
RT   "Crystal structure of echicetin from Echis carinatus (Indian saw-scaled
RT   viper) at 2.4 A resolution.";
RL   J. Mol. Biol. 335:167-176(2004).
CC   -!- FUNCTION: Binding of echicetin to GPIbalpha (GP1BA) receptor on
CC       platelets alone results in inhibition of platelet aggregation, while
CC       binding to both GP1BA receptor and IgMk promotes platelet aggregation
CC       and signal transduction. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:14659748}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
CC   -!- CAUTION: The name echicetin has been given to 2 different proteins,
CC       this one from E.carinatus and another one for which the subspecies has
CC       been specified (E.carinatus sochureki). Most experiments have been done
CC       on E.carinatus sochureki. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP41218.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY268947; AAP41218.2; ALT_INIT; mRNA.
DR   PDB; 1OZ7; X-ray; 2.40 A; A=5-135.
DR   PDBsum; 1OZ7; -.
DR   AlphaFoldDB; Q7T248; -.
DR   SMR; Q7T248; -.
DR   EvolutionaryTrace; Q7T248; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation activating toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT   SIGNAL          <1..4
FT                   /evidence="ECO:0000255"
FT   CHAIN           5..135
FT                   /note="Snaclec echicetin subunit alpha"
FT                   /id="PRO_0000355265"
FT   DOMAIN          13..130
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        6..17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14659748"
FT   DISULFID        34..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14659748"
FT   DISULFID        82
FT                   /note="Interchain (with C-98 in subunit beta)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14659748"
FT   DISULFID        104..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14659748"
FT   NON_TER         1
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          16..25
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   HELIX           27..37
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   HELIX           49..62
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          67..75
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          125..131
FT                   /evidence="ECO:0007829|PDB:1OZ7"
SQ   SEQUENCE   135 AA;  15735 MW;  5095AA5AA7BE5024 CRC64;
     GADEMCPPGW SSNGVYCYML FKEPKTWDEA EKFCNKQGKD GHLLSIESKK EEILVDIVVS
     ENIGKMYKIW TGLSERSKEQ HCSSRWSDGS FFRSYEIAIR YSECFVLEKQ SVFRTWVATP
     CENTFPFMCK YPVPR